ID A0A0R2CRX2_9LACO Unreviewed; 260 AA. AC A0A0R2CRX2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 27-NOV-2024, entry version 27. DE RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915}; DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915}; GN ORFNames=FC56_GL000448 {ECO:0000313|EMBL:KRM93730.1}; OS Lentilactobacillus senioris DSM 24302 = JCM 17472. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lentilactobacillus. OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM93730.1, ECO:0000313|Proteomes:UP000051256}; RN [1] {ECO:0000313|EMBL:KRM93730.1, ECO:0000313|Proteomes:UP000051256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM93730.1, RC ECO:0000313|Proteomes:UP000051256}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J., RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E., RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y., RA Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through comparative RT genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in CC vitro. {ECO:0000256|PIRNR:PIRNR000915}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR000915-3}; CC Note=Divalent metal ions. Mg(2+) is the most effective. CC {ECO:0000256|PIRSR:PIRSR000915-3}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family. CC {ECO:0000256|ARBA:ARBA00006696, ECO:0000256|PIRNR:PIRNR000915}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KRM93730.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AYZR01000008; KRM93730.1; -; Genomic_DNA. DR RefSeq; WP_056978255.1; NZ_AYZR01000008.1. DR AlphaFoldDB; A0A0R2CRX2; -. DR STRING; 1423802.FC56_GL000448; -. DR PATRIC; fig|1423802.4.peg.458; -. DR Proteomes; UP000051256; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IEA:TreeGrafter. DR CDD; cd07530; HAD_Pase_UmpH-like; 1. DR FunFam; 3.40.50.1000:FF:000053; TIGR01457 family HAD hydrolase; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006357; HAD-SF_hydro_IIA. DR InterPro; IPR006354; HAD-SF_hydro_IIA_hyp1. DR InterPro; IPR023214; HAD_sf. DR NCBIfam; TIGR01460; HAD-SF-IIA; 1. DR NCBIfam; TIGR01457; HAD-SF-IIA-hyp2; 1. DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1. DR PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1. DR Pfam; PF13344; Hydrolase_6; 1. DR Pfam; PF13242; Hydrolase_like; 1. DR PIRSF; PIRSF000915; PGP-type_phosphatase; 2. DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1. DR SFLD; SFLDG01139; C2.A:_Pyridoxal_Phosphate_Phos; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 2. DR SUPFAM; SSF56784; HAD-like; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:KRM93730.1}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000915, ECO:0000256|PIRSR:PIRSR000915-3}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000915, KW ECO:0000256|PIRSR:PIRSR000915-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000051256}. FT ACT_SITE 10 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1" FT ACT_SITE 12 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3" FT BINDING 12 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2" FT BINDING 212 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3" SQ SEQUENCE 260 AA; 28599 MW; 34D529750E0F15B0 CRC64; MKQYRGYLID LDGTVYAGTK KIPAAKRFIE RLQQKQIPFL FVTNNSTQLP EAVATNLANN HDIYVNAQNV YTSGMATVDY LNQETKDWPA EDKTVLVVGE YGLKQVILQS GYTLAIDNPA FTVVGLDSDL TYEKLTQAVL AIRNGSRFVG TNPDTNIPKE RGLLPGAGAV VDFVRYATQV EPVMIGKPQA QIINTALRRI NLPATDVVMV GDNYNTDIKA GINAQVDTLL VYTGVSTPEL VAKEAIQPTN FINSLDEWEV //